Distinct structural and mechanical properties of the nuclear lamina in Hutchinson-Gilford progeria syndrome. - Wikidata - wikimedia - TriplyDB

Distinct structural and mechanical properties of the nuclear lamina in Hutchinson-Gilford progeria syndrome.

Distinct structural and mechanical properties of the nuclear lamina in Hutchinson-Gilford progeria syndrome.

http://www.wikidata.org/entity/Q34772038

about

The mutant form of lamin A that causes Hutchinson-Gilford progeria is a biomarker of cellular aging in human skin Mammalian SUN protein interaction networks at the inner nuclear membrane and their role in laminopathy disease processes A-type lamins maintain the positional stability of DNA damage repair foci in mammalian nuclei Model of human aging: recent findings on Werner's and Hutchinson-Gilford progeria syndromes Lamin A-dependent misregulation of adult stem cells associated with accelerated ageing Molecular insights into the premature aging disease progeria Higher order chromatin organization in cancer Joint modeling of cell and nuclear shape variation Nuclear migration events throughout development Implications and Assessment of the Elastic Behavior of Lamins in Laminopathies New approaches for understanding the nuclear force balance in living, adherent cells Laminopathies and the long strange trip from basic cell biology to therapy Prelamin A farnesylation and progeroid syndromes The defective nuclear lamina in Hutchinson-gilford progeria syndrome disrupts the nucleocytoplasmic Ran gradient and inhibits nuclear localization of Ubc9.A progeria mutation reveals functions for lamin A in nuclear assembly, architecture, and chromosome organization.Lamin B counteracts the kinesin Eg5 to restrain spindle pole separation during spindle assembly Transient nuclear envelope rupturing during interphase in human cancer cells.The tethering of chromatin to the nuclear envelope supports nuclear mechanics.Probing cytoskeletal pre-stress and nuclear mechanics in endothelial cells with spatiotemporally controlled (de-)adhesion kinetics on micropatterned substrates.Nonlinear osmotic properties of the cell nucleus.Alpha-helical protein networks are self-protective and flaw-tolerant.Genomic instability and DNA damage responses in progeria arising from defective maturation of prelamin A.Dynamics of lamin-A processing following precursor accumulation.Nuclear localization signal deletion mutants of lamin A and progerin reveal insights into lamin A processing and emerin targeting Diseases of the nuclear envelope.Interactions between nuclei and the cytoskeleton are mediated by SUN-KASH nuclear-envelope bridges.Shear stress-induced mechanotransduction protein deregulation and vasculopathy in a mouse model of progeria.The posttranslational processing of prelamin A and disease.Analyses of the Dynamic Properties of Nuclear Lamins by Fluorescence Recovery After Photobleaching (FRAP) and Fluorescence Correlation Spectroscopy (FCS)How protein materials balance strength, robustness, and adaptability.Mechanobiology and the microcirculation: cellular, nuclear and fluid mechanics.Differential temporal and spatial progerin expression during closure of the ductus arteriosus in neonates Lamin B1 overexpression increases nuclear rigidity in autosomal dominant leukodystrophy fibroblasts.Nuclear lamins.The lamin protein family."Laminopathies": a wide spectrum of human diseases.Cardiovascular pathology in Hutchinson-Gilford progeria: correlation with the vascular pathology of aging.Progeria: translational insights from cell biology.Direct actin binding to A- and B-type lamin tails and actin filament bundling by the lamin A tail.LINCing lamin B2 to neuronal migration: growing evidence for cell-specific roles of B-type lamins.

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Distinct structural and mechanical properties of the nuclear lamina in Hutchinson-Gilford progeria syndrome.

http://www.wikidata.org/entity/Q34772038

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Distinct structural and mechan ...... son-Gilford progeria syndrome.

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Proceedings of the National Academy of Sciences of the United States of America

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Distinct structural and mechan ...... son-Gilford progeria syndrome.

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Arjun G Yodh

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Katherine L Wilson

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Kris Noel Dahl

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Mohammad F Islam

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Paola Scaffidi

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Tom Misteli

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P2860

Nuclear lamins: building blocks of nuclear architecture

Reversal of the cellular phenotype in the premature aging disease Hutchinson-Gilford progeria syndrome

Accumulation of mutant lamin A causes progressive changes in nuclear architecture in Hutchinson-Gilford progeria syndrome

Nuclear pore complexes form immobile networks and have a very low turnover in live mammalian cells

Recurrent de novo point mutations in lamin A cause Hutchinson-Gilford progeria syndrome

Life at the edge: the nuclear envelope and human disease

Genomic instability in laminopathy-based premature aging

Abnormal nuclear shape and impaired mechanotransduction in emerin-deficient cells

High mobility of proteins in the mammalian cell nucleus

Nuclear protein import in permeabilized mammalian cells requires soluble cytoplasmic factors

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